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Yorodumi- PDB-1jli: HUMAN INTERLEUKIN 3 (IL-3) MUTANT WITH TRUNCATION AT BOTH N-AND C... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jli | ||||||
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Title | HUMAN INTERLEUKIN 3 (IL-3) MUTANT WITH TRUNCATION AT BOTH N-AND C-TERMINI AND 14 RESIDUE CHANGES, NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
Components | INTERLEUKIN 3 | ||||||
Keywords | CYTOKINE / HEMATOPOIETIC GROWTH FACTOR / COLONY-STIMULATING FACTOR | ||||||
Function / homology | Function and homology information interleukin-3 receptor binding / RUNX1 regulates transcription of genes involved in interleukin signaling / interleukin-3-mediated signaling pathway / embryonic hemopoiesis / Interleukin-3, Interleukin-5 and GM-CSF signaling / Interleukin receptor SHC signaling / positive regulation of tyrosine phosphorylation of STAT protein / cytokine activity / growth factor activity / positive regulation of peptidyl-tyrosine phosphorylation ...interleukin-3 receptor binding / RUNX1 regulates transcription of genes involved in interleukin signaling / interleukin-3-mediated signaling pathway / embryonic hemopoiesis / Interleukin-3, Interleukin-5 and GM-CSF signaling / Interleukin receptor SHC signaling / positive regulation of tyrosine phosphorylation of STAT protein / cytokine activity / growth factor activity / positive regulation of peptidyl-tyrosine phosphorylation / cell-cell signaling / nervous system development / RAF/MAP kinase cascade / immune response / positive regulation of cell population proliferation / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Feng, Y. / Klein, B.K. / Mcwherter, C.A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996 Title: Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3. Authors: Feng, Y. / Klein, B.K. / McWherter, C.A. #1: Journal: Biochemistry / Year: 1995 Title: 1H, 13C, and 15N NMR Resonance Assignments, Secondary Structure, and Backbone Topology of a Variant of Human Interleukin-3 Authors: Feng, Y. / Klein, B.K. / Vu, L. / Aykent, S. / Mcwherter, C.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jli.cif.gz | 47.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jli.ent.gz | 37.6 KB | Display | PDB format |
PDBx/mmJSON format | 1jli.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jli_validation.pdf.gz | 244.5 KB | Display | wwPDB validaton report |
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Full document | 1jli_full_validation.pdf.gz | 244.3 KB | Display | |
Data in XML | 1jli_validation.xml.gz | 4.3 KB | Display | |
Data in CIF | 1jli_validation.cif.gz | 5.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jl/1jli ftp://data.pdbj.org/pub/pdb/validation_reports/jl/1jli | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12844.856 Da / Num. of mol.: 1 Mutation: DEL(1-13), V14A, N18I, T25H, Q29R, L32N, F37P, G42S, Q45M, N51R, R55T, E59L, N62V, S67H, Q69E, DEL(126-133) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PMON 13302 / Production host: Escherichia coli (E. coli) / Strain (production host): JM101 / References: UniProt: P08700 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Software |
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NMR software | Name: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement | ||||||||||||
Refinement | Software ordinal: 1 Details: AS IN X-PLOR PARALLHDG.PRO STRUCTURES WERE CALCULATED USING A SIMULATED ANNEALING PROTOCOL IN X-PLOR. INPUT CONSTRAINTS ARE AS FOLLOWS: 1659 NUCLEAR OVERHAUSER ENHANCEMENT (NOE) (799 INTRA- ...Details: AS IN X-PLOR PARALLHDG.PRO STRUCTURES WERE CALCULATED USING A SIMULATED ANNEALING PROTOCOL IN X-PLOR. INPUT CONSTRAINTS ARE AS FOLLOWS: 1659 NUCLEAR OVERHAUSER ENHANCEMENT (NOE) (799 INTRA-RESIDUE; 342 SEQUENTIAL (I-J =1); 236 MEDIUM-RANGE INTERRESIDUE (<1 I-J <=5); 282 LONG-RANGE INTERRESIDUE (I-J >5)); 38 PAIRS OF HYDROGEN-BOND RESTRAINTS; 76 PHI TORSION ANGLE RESTRAINTS. PSEUDOATOM POSITIONS WERE USED FOR CONSTRAINTS INVOLVING METHYLENE, AROMATIC, AND METHYL PROTONS. THE COORDINATES DEPOSITED HERE ARE OBTAINED BY AVERAGING 25 CONVERGED STRUCTURES PRIOR TO A RESTRAINED ENERGY MINIMIZATION. A COMPARISON OF THE FAMILY OF THE 25 STRUCTURES WITH THE AVERAGED STRUCTURE GIVES RMSD VALUES OF 0.88 ANGSTROMS FOR ALL (N,CA,C') EXCEPT RESIDUES 28 - 39, AND 0.41 ANGSTROMS FOR (N,CA,C') OF HELICAL REGIONS (RESIDUES 16 - 26, 42 - 49, 54 - 67, 72 - 84, AND 104 - 122). | ||||||||||||
NMR ensemble | Conformers submitted total number: 1 |